• Users Online: 102
  • Print this page
  • Email this page
 
ORIGINAL ARTICLE
Ahead of Print

Targeting of interleukin-10 receptor by a potential human interleukin-10 peptide efficiently blocks interleukin-10 pathway-dependent cell proliferation


1 Department of Laboratory Medicine, Hualien Tzu Chi Hospital, Buddhist Tzu Chi Medical Foundation, Hualien, Taiwan
2 Institute of Medical Sciences, Tzu Chi University, Hualien, Taiwan
3 Department of Biochemistry, School of Medicine, Tzu Chi University, Hualien, Taiwan
4 Department of Oncology and Hematology, Hualien Tzu Chi Hospital, Buddhist Tzu Chi Medical Foundation, Hualien, Taiwan
5 Department of Biochemistry, School of Medicine, Tzu Chi University; Department of Life Sciences, Tzu Chi University, Hualien, Taiwan

Correspondence Address:
Chih-Wen Peng,
Institute of Medical Sciences, Tzu Chi University, Hualien
Taiwan
Hao-Jen Hsu,
Department of Life Sciences, Tzu Chi University, 701, Section 3, Zhongyang Road, Hualien
Taiwan
Login to access the Email id

Source of Support: None, Conflict of Interest: None

DOI: 10.4103/tcmj.tcmj_237_19

Objective: Human interleukin-10 (IL-10) is a dimeric and pleiotropic cytokine that plays a crucial role in cellular immunoregulatory responses. As IL-10 binds to its receptors, IL-10Ra and IL-10Rb, it will suppress or induce the downstream cellular immune responses to protect from diseases. Materials and Methods: In this study, a potential peptide derived from IL-10 based on molecular docking and structural analysis was designed and validated by a series of cell assays to block IL-10 binding to receptor IL-10Ra for the inhibition of cell growth. Results: The simulation results indicate that the designed peptide IL10NM25 bound to receptor IL-10Ra is dominated by electrostatic interactions, whereas van der Waals (VDW) and hydrophobic interactions are minor. The cell experiments showed that IL10NM25 specifically binds to receptor IL-10Ra on the cell surface of two B-lineage cell lines, B lymphoma derived (BJAB), and lymphoblastoid cell line, whereas the mutant and scramble peptides are not able to suppress the binding of IL-10 to receptor IL-10Ra, consistent with the molecular simulation predictions. Conclusions: This study demonstrates that structure-based peptide design can be effective in the development of peptide drug discovery.


Print this article
Search
 Back
 
  Search Pubmed for
 
    -  Chang CC
    -  Liu CD
    -  Pan SF
    -  Huang WH
    -  Peng CW
    -  Hsu HJ
 Citation Manager
 Article Access Statistics
 Reader Comments
 * Requires registration (Free)
 

 Article Access Statistics
    Viewed163    
    PDF Downloaded10    

Recommend this journal